issue contents
December 2021 issue
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Cover illustration: Structure of mitogen-activated protein kinase kinase 1 in the DFG-out conformation [Nakae et al. (2021), Acta Cryst. F77, 459–464]. Eukaryotic protein kinases contain an Asp-Phe-Gly (DFG) motif, the conformation of which is involved in controlling the catalytic activity and can be switched between active-state (DFG-in) and inactive-state (DFG-out) conformations. The mechanism of conformational change is poorly understood, partly because there are few reports of the DFG-out conformation. Here, a novel crystal structure of nonphosphorylated human mitogen-activated protein kinase kinase 1 complexed with ATP-γS is reported in which MEK1 adopts the DFG-out conformation.
editorial
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research communications
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